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- W1623867701 abstract "Extracellular adenosine acts as a neuromodulator through two subtypes of membrane-bound receptors. At each receptor subtype, xanthines act as competitive antagonists. This chapter describes a study in which a range of chain lengths separating biotin and adenosine pharmacophore moieties was synthesized. Spacer groups consisting of ɛ-aminocaproic acid and oligoglycine were utilized. The ɛ-biotinyl-D-amino acid isomer was included to minimize proteolytic cleavage, a potential problem in biological assay systems. In the form of avidin complexes, the xanthine conjugates lost their affinity for the receptor, which suggested conformational or topographical differences between agonist- and antagonist-occupied receptors. Ethyl acetate and 0.1 M HCI were added, and the phases were mixed. The upper phase was washed with water and evaporated and the residue was triturated with ethyl acetate and petroleum ether. Structure–activity relationships for adenosine agonists and antagonists were examined initially to identify potential sites for derivatization. Because neither adenosine nor theophylline contains a readily derivatized functional group that is nonessential for biological activity, a functionalized congener methodology was used." @default.
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- W1623867701 date "1990-01-01" @default.
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- W1623867701 title "[79] Probing adenosine receptors using biotinylated purine derivatives" @default.
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- W1623867701 doi "https://doi.org/10.1016/0076-6879(90)84333-c" @default.
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